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Structure of histone acetyltransferases.

R Marmorstein1

  • 1The Wistar Institute and the Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA. marmor@wistar.upenn.edu

Journal of Molecular Biology
|August 9, 2001
PubMed
Summary

Histone acetyltransferase (HAT) enzymes regulate gene activation by acetylating histones. Structural analysis reveals a conserved core domain for catalysis and variable terminal domains for substrate binding across diverse HAT families.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • Histone acetyltransferase (HAT) enzymes are crucial for gene regulation.
  • HATs acetylate histone N-terminal regions, promoting chromatin accessibility and gene activation.
  • Over 20 HAT members exist, categorized into families with conserved functions and divergent specificities.

Purpose of the Study:

  • To elucidate the structural basis of catalysis and substrate binding in diverse HAT enzymes.
  • To compare the structures of distinct HAT families (Hat1, Gcn5/PCAF, Esa1).
  • To correlate structural features with functional roles in histone acetylation.

Main Methods:

  • X-ray crystallography for structure determination of Hat1, Gcn5/PCAF, and Esa1.
  • Comparative structural analysis of conserved and divergent domains.
  • Integration of structural data with existing biochemical and functional studies.

Main Results:

  • A conserved central core domain was identified across divergent HAT enzymes.
  • This core domain interacts extensively with the acetyl-coenzyme A cofactor.
  • Structurally distinct N- and C-terminal domains were observed, varying between HAT families.

Conclusions:

  • The core domain is critical for HAT catalytic activity.
  • N- and C-terminal domains are important for specific histone substrate binding.
  • A conserved catalytic and substrate binding mechanism is implied across diverse HAT enzymes.

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